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 Blood, 15 December 2005, Vol. 106, No. 13, pp. 4146-4151.
Prepublished online as a Blood First Edition Paper on August 16, 2005; DOI 10.1182/blood-2005-03-1223.

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HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY

Role of FcR{gamma} and factor XIIIA in coated platelet formation

Shawn M. Jobe, Lorie Leo, Joshua S. Eastvold, Gerhard Dickneite, Timothy L. Ratliff, Steven R. Lentz, and Jorge Di Paola

From the Departments of Pediatrics, Internal Medicine, and Urology, University of Iowa College of Medicine, Iowa City, IA; ZLB Behring, Marburg, Germany; and Veterans Affairs Medical Center, Iowa City, IA.

Platelet activation in response to dual stimulation with collagen and thrombin results in the formation of a subpopulation of activated platelets known as coated platelets. Coated platelets are characterized by high surface levels of {alpha}-granule proteins and phosphatidylserine, which support the assembly of procoagulant protein complexes. Using murine models, we tested the hypothesis that the collagen receptor-associated molecule FcR{gamma} and the transglutaminase factor XIIIA are required for the formation of coated platelets. Following dual stimulation with the collagen receptor agonist convulxin and thrombin, 68% of platelets from C57BL/6 mice acquired the coated platelet phenotype, defined by high surface levels of fibrinogen and von Willebrand factor and decreased binding of the {alpha}IIb{beta}3 activation-dependent antibody PE-JON/A. In FcR{gamma}-/- mice, only 10% of platelets became "coated" after dual stimulation with convulxin plus thrombin (P < .05 vs C57BL/6 platelets). Decreased coated platelet formation in FcR{gamma}-/- platelets was accompanied by decreased annexin V binding (P < .01) and decreased platelet procoagulant activity (P < .05). Platelets from FXIIIA-/- mice did not differ from control platelets in coated platelet formation or annexin V binding. We conclude that FcR{gamma}, but not factor XIIIA, is essential for formation of highly procoagulant coated platelets following dual stimulation with collagen and thrombin.


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